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Volumn 1770, Issue 8, 2007, Pages 1248-1258

Molecular modeling and functional analysis of the AtoS-AtoC two-component signal transduction system of Escherichia coli

Author keywords

54 regulator factor; Antizyme; AtoC; AtoS; ATPase; DNA binding; Structural model; Two component system

Indexed keywords

ASPARTIC ACID; HISTIDINE; PHOSPHATE; PROTEIN ATOC; PROTEIN ATOS; PROTEIN DERIVATIVE; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 34347233816     PISSN: 03044165     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbagen.2007.04.004     Document Type: Article
Times cited : (22)

References (51)
  • 1
    • 0031589010 scopus 로고    scopus 로고
    • Compilation of all genes encoding two-component phosphotransfer signal transducers in the genome of Escherichia coli
    • Mizuno T. Compilation of all genes encoding two-component phosphotransfer signal transducers in the genome of Escherichia coli. DNA Res. 4 (1997) 161-168
    • (1997) DNA Res. , vol.4 , pp. 161-168
    • Mizuno, T.1
  • 2
    • 0035369115 scopus 로고    scopus 로고
    • Histidine kinases and response regulator proteins in two-component signalling systems
    • West A.H., and Stock A.M. Histidine kinases and response regulator proteins in two-component signalling systems. Trends Biochem. Sci. 26 (2001) 369-376
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 369-376
    • West, A.H.1    Stock, A.M.2
  • 4
    • 0015523712 scopus 로고
    • ato operon: a highly inducible system for acetoacetate and butyrate degradation in Escherichia coli
    • Pauli G., and Overath P. ato operon: a highly inducible system for acetoacetate and butyrate degradation in Escherichia coli. Eur. J. Biochem. 29 (1972) 553-562
    • (1972) Eur. J. Biochem. , vol.29 , pp. 553-562
    • Pauli, G.1    Overath, P.2
  • 5
    • 0023089497 scopus 로고
    • Genetic and molecular characterization of the genes involved in short-chain fatty acid degradation in Escherichia coli: the ato system
    • Jenkins L.S., and Nunn W.D. Genetic and molecular characterization of the genes involved in short-chain fatty acid degradation in Escherichia coli: the ato system. J. Bacteriol. 169 (1987) 42-52
    • (1987) J. Bacteriol. , vol.169 , pp. 42-52
    • Jenkins, L.S.1    Nunn, W.D.2
  • 6
    • 0023213801 scopus 로고
    • Regulation of the ato operon by the atoC gene in Escherichia coli
    • Jenkins L.S., and Nunn W.D. Regulation of the ato operon by the atoC gene in Escherichia coli. J. Bacteriol. 169 (1987) 2096-2102
    • (1987) J. Bacteriol. , vol.169 , pp. 2096-2102
    • Jenkins, L.S.1    Nunn, W.D.2
  • 7
    • 0017283631 scopus 로고
    • The appearance of an ornithine decarboxylase inhibitory protein upon the addition of putrescine to cell cultures
    • Fong W.F., Heller J.S., and Canellakis E.S. The appearance of an ornithine decarboxylase inhibitory protein upon the addition of putrescine to cell cultures. Biochim. Biophys. Acta 428 (1976) 456-465
    • (1976) Biochim. Biophys. Acta , vol.428 , pp. 456-465
    • Fong, W.F.1    Heller, J.S.2    Canellakis, E.S.3
  • 8
    • 0345955882 scopus 로고
    • Induction of a protein inhibitor of ornithine decarboxylase by the end products of its reaction
    • Heller J.S., Fong W.F., and Canellakis E.S. Induction of a protein inhibitor of ornithine decarboxylase by the end products of its reaction. Proc. Natl. Acad. Sci. U. S. A. 73 (1976) 1858-1862
    • (1976) Proc. Natl. Acad. Sci. U. S. A. , vol.73 , pp. 1858-1862
    • Heller, J.S.1    Fong, W.F.2    Canellakis, E.S.3
  • 9
    • 0011999529 scopus 로고
    • Modulation of ornithine decarboxylase activity in Escherichia coli by positive and negative effectors
    • Kyriakidis D.A., Heller J.S., and Canellakis E.S. Modulation of ornithine decarboxylase activity in Escherichia coli by positive and negative effectors. Proc. Natl. Acad. Sci. U. S. A. 75 (1978) 4699-4703
    • (1978) Proc. Natl. Acad. Sci. U. S. A. , vol.75 , pp. 4699-4703
    • Kyriakidis, D.A.1    Heller, J.S.2    Canellakis, E.S.3
  • 12
    • 0043032929 scopus 로고    scopus 로고
    • Phenotype Microarray analysis of Escherichia coli K-12 mutants with deletions of all two-component systems
    • Zhou L., Lei X.-H., Bochner B.R., and Wanner B.L. Phenotype Microarray analysis of Escherichia coli K-12 mutants with deletions of all two-component systems. J. Bacteriol. 185 (2003) 4956-4972
    • (2003) J. Bacteriol. , vol.185 , pp. 4956-4972
    • Zhou, L.1    Lei, X.-H.2    Bochner, B.R.3    Wanner, B.L.4
  • 13
    • 33744509542 scopus 로고    scopus 로고
    • Involvement of the AtoS-AtoC signal transduction system in poly-(R)-3-hydroxybutyrate biosynthesis in Escherichia coli
    • Theodorou M.C., Panagiotidis C.A., Panagiotidis C.H., Pantazaki A.A., and Kyriakidis D.A. Involvement of the AtoS-AtoC signal transduction system in poly-(R)-3-hydroxybutyrate biosynthesis in Escherichia coli. Biochim. Biophys. Acta 1760 (2006) 896-906
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 896-906
    • Theodorou, M.C.1    Panagiotidis, C.A.2    Panagiotidis, C.H.3    Pantazaki, A.A.4    Kyriakidis, D.A.5
  • 14
    • 12544258487 scopus 로고    scopus 로고
    • Functional characterization in vitro of all two-component signal transduction systems from Escherichia coli
    • Yamamoto K., Hirao K., Oshima T., Aiba H., Utsumi R., and Ishihama A. Functional characterization in vitro of all two-component signal transduction systems from Escherichia coli. J. Biol. Chem. 280 (2005) 1448-1456
    • (2005) J. Biol. Chem. , vol.280 , pp. 1448-1456
    • Yamamoto, K.1    Hirao, K.2    Oshima, T.3    Aiba, H.4    Utsumi, R.5    Ishihama, A.6
  • 15
    • 12144284818 scopus 로고    scopus 로고
    • The role of bacterial antizyme: From an inhibitory protein to AtoC transcriptional regulator
    • Lioliou E.E., and Kyriakidis D.A. The role of bacterial antizyme: From an inhibitory protein to AtoC transcriptional regulator. Microb. Cell Fact. 3 (2004) 8-16
    • (2004) Microb. Cell Fact. , vol.3 , pp. 8-16
    • Lioliou, E.E.1    Kyriakidis, D.A.2
  • 16
    • 0025490244 scopus 로고
    • Transmembrane signal transduction and osmoregulation in Escherichia coli: II. The osmotic sensor, EnvZ, located in the isolated cytoplasmic membrane displays its phosphorylation and dephoshorylation abilities as to the activator protein, OmpR
    • Tokishita S.I., Yamada H., Aiba H., and Mizuno T. Transmembrane signal transduction and osmoregulation in Escherichia coli: II. The osmotic sensor, EnvZ, located in the isolated cytoplasmic membrane displays its phosphorylation and dephoshorylation abilities as to the activator protein, OmpR. J. Biochem. 108 (1990) 488-493
    • (1990) J. Biochem. , vol.108 , pp. 488-493
    • Tokishita, S.I.1    Yamada, H.2    Aiba, H.3    Mizuno, T.4
  • 17
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein binding. Anal. Biochem. 72 (1976) 248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 18
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from acrylamide gels to nitrocellulose sheets: procedure and some applications
    • Towbin H., Staehelin T., and Gordon J. Electrophoretic transfer of proteins from acrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. U. S. A. 76 (1979) 4350-4354
    • (1979) Proc. Natl. Acad. Sci. U. S. A. , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 19
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond.) 227 (1970) 680-685
    • (1970) Nature (Lond.) , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 20
    • 0018258229 scopus 로고
    • A sensitive and precise isotopic assay of ATPase activity
    • Seals J.M., McDonald J.M., Bruns D., and Jarett L. A sensitive and precise isotopic assay of ATPase activity. Anal. Biochem. 90 (1978) 785-795
    • (1978) Anal. Biochem. , vol.90 , pp. 785-795
    • Seals, J.M.1    McDonald, J.M.2    Bruns, D.3    Jarett, L.4
  • 21
    • 0028832266 scopus 로고
    • Characterization of the nucleotide binding properties and ATPase activity of recombinant hamster BiP purified from bacteria
    • Wei J., and Hendershot L.M. Characterization of the nucleotide binding properties and ATPase activity of recombinant hamster BiP purified from bacteria. J. Biol. Chem. 270 (1995) 26670-26676
    • (1995) J. Biol. Chem. , vol.270 , pp. 26670-26676
    • Wei, J.1    Hendershot, L.M.2
  • 22
    • 0031022820 scopus 로고    scopus 로고
    • Physical and functional interactions between herpes simplex virus immediate-early proteins ICP4 and ICP27
    • Panagiotidis C.A., Lium E.K., and Silverstein S.J. Physical and functional interactions between herpes simplex virus immediate-early proteins ICP4 and ICP27. J. Virol. 71 (1997) 1547-1557
    • (1997) J. Virol. , vol.71 , pp. 1547-1557
    • Panagiotidis, C.A.1    Lium, E.K.2    Silverstein, S.J.3
  • 24
    • 0033957834 scopus 로고    scopus 로고
    • The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000
    • Bairoch A., and Apweiler R. The SWISS-PROT protein sequence database and its supplement TrEMBL in 2000. Nucleic Acids Res. 28 (2000) 45-48
    • (2000) Nucleic Acids Res. , vol.28 , pp. 45-48
    • Bairoch, A.1    Apweiler, R.2
  • 27
    • 0034623005 scopus 로고    scopus 로고
    • T-Coffee: a novel method for multiple sequence alignments
    • Notredame C., Higgins D., and Heringa J. T-Coffee: a novel method for multiple sequence alignments. J. Mol. Biol. 302 (2000) 205-217
    • (2000) J. Mol. Biol. , vol.302 , pp. 205-217
    • Notredame, C.1    Higgins, D.2    Heringa, J.3
  • 28
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modelling
    • Guex N., and Peitsch M.C. SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modelling. Electrophoresis 18 (1997) 2714-2723
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 31
    • 0344436666 scopus 로고    scopus 로고
    • The yeast Ypd1/Sln1 complex. Insights into molecular recognition in two-component signaling systems
    • Xu Q., Porter S.W., and West A.H. The yeast Ypd1/Sln1 complex. Insights into molecular recognition in two-component signaling systems. Structure (Camb) 11 (2003) 1569-1581
    • (2003) Structure (Camb) , vol.11 , pp. 1569-1581
    • Xu, Q.1    Porter, S.W.2    West, A.H.3
  • 33
  • 34
    • 0003845223 scopus 로고    scopus 로고
    • DeLano Scientific, San Carlos, CA, USA http://www.pymol.org
    • DeLano W.L. The PyMOL Molecular Graphics System (2002), DeLano Scientific, San Carlos, CA, USA. http://www.pymol.org http://www.pymol.org
    • (2002) The PyMOL Molecular Graphics System
    • DeLano, W.L.1
  • 35
    • 0029609746 scopus 로고
    • Phosphotransfer circuitry of the putative multi-signal transducer, ArcB, of Escherichia coli: in vitro studies with mutants
    • Tsuzuki M., Shige K., and Mizuno T. Phosphotransfer circuitry of the putative multi-signal transducer, ArcB, of Escherichia coli: in vitro studies with mutants. Mol. Microbiol. 18 (1995) 953-962
    • (1995) Mol. Microbiol. , vol.18 , pp. 953-962
    • Tsuzuki, M.1    Shige, K.2    Mizuno, T.3
  • 38
  • 40
    • 0037332383 scopus 로고    scopus 로고
    • Domain architectures of sigma54-dependent transcriptional activators
    • Studholme D.J., and Dixon R. Domain architectures of sigma54-dependent transcriptional activators. J. Bacteriol. 185 (2003) 1757-1767
    • (2003) J. Bacteriol. , vol.185 , pp. 1757-1767
    • Studholme, D.J.1    Dixon, R.2
  • 41
    • 0026070143 scopus 로고
    • The phosphorylated form of the enhancer-binding protein NTRC has ATPase activity that is essential for activation of transcription
    • Weiss D.S., Batut J., Klose K.E., Keener J., and Kustu S. The phosphorylated form of the enhancer-binding protein NTRC has ATPase activity that is essential for activation of transcription. Cell 67 (1991) 155-167
    • (1991) Cell , vol.67 , pp. 155-167
    • Weiss, D.S.1    Batut, J.2    Klose, K.E.3    Keener, J.4    Kustu, S.5
  • 42
    • 0026512864 scopus 로고
    • Phosphorylation of bacterial response regulator proteins by low molecular weight phospho-donors
    • Lukat G.S., McCleary W.R., Stock A.M., and Stock J.B. Phosphorylation of bacterial response regulator proteins by low molecular weight phospho-donors. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 718-722
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 718-722
    • Lukat, G.S.1    McCleary, W.R.2    Stock, A.M.3    Stock, J.B.4
  • 43
    • 0030591808 scopus 로고    scopus 로고
    • Regulation of the Escherichia coli biosynthetic ornithine decarboxylase activity by phosphorylation and nucleotides
    • Anagnostopoulos C.G., and Kyriakidis D.A. Regulation of the Escherichia coli biosynthetic ornithine decarboxylase activity by phosphorylation and nucleotides. Biochim. Biophys. Acta 1297 (1996) 228-234
    • (1996) Biochim. Biophys. Acta , vol.1297 , pp. 228-234
    • Anagnostopoulos, C.G.1    Kyriakidis, D.A.2
  • 44
    • 84959062091 scopus 로고    scopus 로고
    • Two-carbon compounds and fatty acids as carbon sources
    • Neidhardt F.C. (Ed), American Society of Microbiology, Washington, D.C.
    • Clark Jr. D.P., and Cronan J.E. Two-carbon compounds and fatty acids as carbon sources. In: Neidhardt F.C. (Ed). Escherichia coli and Salmonella typhimurium (Cellular and Molecular Biology) vol. 1 (1996), American Society of Microbiology, Washington, D.C. 343-357
    • (1996) Escherichia coli and Salmonella typhimurium (Cellular and Molecular Biology) , vol.1 , pp. 343-357
    • Clark Jr., D.P.1    Cronan, J.E.2
  • 45
    • 0029166594 scopus 로고
    • The bacterial enhancer-binding protein NTRC is a molecular machine: ATP hydrolysis is coupled to transcriptional activation
    • Wedel A., and Kustu S. The bacterial enhancer-binding protein NTRC is a molecular machine: ATP hydrolysis is coupled to transcriptional activation. Genes Dev. 9 (1995) 2042-2052
    • (1995) Genes Dev. , vol.9 , pp. 2042-2052
    • Wedel, A.1    Kustu, S.2
  • 46
    • 0033912262 scopus 로고    scopus 로고
    • The bacterial enhancer-dependent sigma (54) (sigma N) transcription factor
    • Buck M., Gallegos M.T., Studholme D.J., Guo Y., and Gralla J.D. The bacterial enhancer-dependent sigma (54) (sigma N) transcription factor. J. Bacteriol. 182 (2000) 4129-4136
    • (2000) J. Bacteriol. , vol.182 , pp. 4129-4136
    • Buck, M.1    Gallegos, M.T.2    Studholme, D.J.3    Guo, Y.4    Gralla, J.D.5
  • 47
    • 0029016807 scopus 로고
    • Constitutive forms of the enhancer-binding protein NtrC: evidence that essential oligomerization determinants lie in the central activation domain
    • Flashner Y., Weiss D.S., Keener J., and Kustu S. Constitutive forms of the enhancer-binding protein NtrC: evidence that essential oligomerization determinants lie in the central activation domain. J. Mol. Biol. 249 (1995) 700-713
    • (1995) J. Mol. Biol. , vol.249 , pp. 700-713
    • Flashner, Y.1    Weiss, D.S.2    Keener, J.3    Kustu, S.4
  • 48
    • 0026773062 scopus 로고
    • Phosphorylation of nitrogen regulator I of Escherichia coli induces strong cooperative binding to DNA essential for activation of transcription
    • Weiss V., Claverie-Martin F., and Magasanik B. Phosphorylation of nitrogen regulator I of Escherichia coli induces strong cooperative binding to DNA essential for activation of transcription. Proc. Natl. Acad. Sci. U. S. A. 89 (1992) 5088-5092
    • (1992) Proc. Natl. Acad. Sci. U. S. A. , vol.89 , pp. 5088-5092
    • Weiss, V.1    Claverie-Martin, F.2    Magasanik, B.3
  • 49
    • 0032538615 scopus 로고    scopus 로고
    • Properties of a mutant form of the prokaryotic enhancer binding protein, NTRC, which hydrolyses ATP in the absence of effectors
    • Widdick D., Farez-Vidal1 E., Austin S., and Dixon R. Properties of a mutant form of the prokaryotic enhancer binding protein, NTRC, which hydrolyses ATP in the absence of effectors. FEBS Lett. 437 (1998) 70-74
    • (1998) FEBS Lett. , vol.437 , pp. 70-74
    • Widdick, D.1    Farez-Vidal1, E.2    Austin, S.3    Dixon, R.4
  • 50
    • 0026581288 scopus 로고
    • The procaryotic enhancer binding protein NTRC has an ATPase activity which is phosphorylation and DNA dependent
    • Austin S., and Dixon R. The procaryotic enhancer binding protein NTRC has an ATPase activity which is phosphorylation and DNA dependent. EMBO J. 11 (1992) 2219-2228
    • (1992) EMBO J. , vol.11 , pp. 2219-2228
    • Austin, S.1    Dixon, R.2


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